1NI2

Structure of the active FERM domain of Ezrin

1NI2 の概要

• エントリーDOI: 10.2210/pdb1ni2/pdb
• 分子名称: Ezrin (2 entities in total)
• 機能のキーワード: ferm, keystone, ubiquitin-like domain, acyl-coa-like domain, ph/ptb-like domain, structural protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Apical cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P15311
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69896.79

構造登録者

Smith, W.J.,Nassar, N.,Bretscher, A.P.,Cerione, R.A.,Karplus, P.A. (登録日: 2002-12-20, 公開日: 2003-02-25, 最終更新日: 2023-08-16)

主引用文献

Smith, W.J.,Nassar, N.,Bretscher, A.P.,Cerione, R.A.,Karplus, P.A.
Structure of the Active N-terminal Domain of Ezrin. CONFORMATIONAL AND MOBILITY CHANGES IDENTIFY KEYSTONE INTERACTIONS.
J.Biol.Chem., 278:4949-4956, 2003

PubMed Abstract: Ezrin is a member of the ERM (ezrin, radixin, moesin) family of proteins that cross-link the actin cytoskeleton to the plasma membrane and also may function in signaling cascades that regulate the assembly of actin stress fibers. Here, we report a crystal structure for the free (activated) FERM domain (residues 2-297) of recombinant human ezrin at 2.3 A resolution. Structural comparison among the dormant moesin FERM domain structure and the three known active FERM domain structures (radixin, moesin, and now ezrin) allows the clear definition of regions that undergo structural changes during activation. The key regions affected are residues 135-150 and 155-180 in lobe F2 and residues 210-214 and 235-267 in lobe F3. Furthermore, we show that a large increase in the mobilities of lobes F2 and F3 accompanies activation, suggesting that their integrity is compromised. This leads us to propose a new concept that we refer to as keystone interactions. Keystone interactions occur when one protein (or protein part) contributes residues that allow another protein to complete folding, meaning that it becomes an integral part of the structure and would rarely dissociate. Such interactions are well suited for long-lived cytoskeletal protein interactions. The keystone interactions concept leads us to predict two specific docking sites within lobes F2 and F3 that are likely to bind target proteins.

PubMed: 12429733
DOI: 10.1074/jbc.M210601200

実験手法

X-RAY DIFFRACTION (2.3 Å)